BRENDA - Enzyme Database show
show all sequences of 1.6.3.5

Renalase does not catalyze the oxidation of catecholamines

Beaupre, B.A.; Hoag, M.R.; Moran, G.R.; Arch. Biochem. Biophys. 579, 62-66 (2015)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1,2-dihydro-beta-NADH + H+ + O2
Homo sapiens
-
beta-NAD+ + H2O2
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
Homo sapiens
-
beta-NADP+ + H2O2
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
Homo sapiens
-
beta-NAD+ + H2O2
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
Homo sapiens
-
beta-NADP+ + H2O2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
blood plasma
-
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,2-dihydro-beta-NADH + H+ + O2
-
741775
Homo sapiens
beta-NAD+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
-
741775
Homo sapiens
beta-NADP+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
-
741775
Homo sapiens
beta-NAD+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
-
741775
Homo sapiens
beta-NADP+ + H2O2
-
-
-
?
additional information
renalase does not catalyze the oxidation of catecholamines
741775
Homo sapiens
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Homo sapiens
NADH
-
Homo sapiens
NADPH
-
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Homo sapiens
NADH
-
Homo sapiens
NADPH
-
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1,2-dihydro-beta-NADH + H+ + O2
Homo sapiens
-
beta-NAD+ + H2O2
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
Homo sapiens
-
beta-NADP+ + H2O2
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
Homo sapiens
-
beta-NAD+ + H2O2
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
Homo sapiens
-
beta-NADP+ + H2O2
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
blood plasma
-
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,2-dihydro-beta-NADH + H+ + O2
-
741775
Homo sapiens
beta-NAD+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
-
741775
Homo sapiens
beta-NADP+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
-
741775
Homo sapiens
beta-NAD+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
-
741775
Homo sapiens
beta-NADP+ + H2O2
-
-
-
?
additional information
renalase does not catalyze the oxidation of catecholamines
741775
Homo sapiens
?
-
-
-
-
Other publictions for EC 1.6.3.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741788
Moran
The enzyme Renalase ...
Homo sapiens, Pseudomonas savastanoi 1448A, Pseudomonas savastanoi
Arch. Biochem. Biophys.
632
66-76
2017
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12
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3
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4
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17
2
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12
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4
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17
2
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742961
Wang
Extracellular renalase protec ...
Homo sapiens
J. Cell. Mol. Med.
21
1260-1265
2017
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1
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1
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1
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1
2
2
1
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-
741785
Beaupre
Ligand binding phenomena that ...
Pseudomonas savastanoi pv. phaseolicola 1448A, Pseudomonas savastanoi pv. phaseolicola
Arch. Biochem. Biophys.
612
46-56
2016
1
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10
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8
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4
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16
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3
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1
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3
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10
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8
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16
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741869
Severina
The history of renalase from ...
Homo sapiens
Biochemistry (Moscow)
10
97-109
2016
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4
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1
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2
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8
1
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3
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3
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4
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8
1
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742004
Moran
The catalytic function of ren ...
Homo sapiens
Biochim. Biophys. Acta
1864
177-186
2016
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7
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2
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1
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4
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7
1
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3
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3
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7
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1
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4
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7
1
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743189
Fedchenko
Renalase secreted by human ki ...
Homo sapiens
Kidney Blood Press. Res.
41
593-603
2016
-
-
-
-
-
-
-
-
1
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2
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2
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1
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1
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1
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1
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2
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1
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741574
Quelhas-Santos
Renalase regulates peripheral ...
Mus musculus
Am. J. Physiol. Renal Physiol.
308
F84-F91
2015
-
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-
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-
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4
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1
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1
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2
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2
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1
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1
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741775
Beaupre
Renalase does not catalyze th ...
Homo sapiens
Arch. Biochem. Biophys.
579
62-66
2015
-
-
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-
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4
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2
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2
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5
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3
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3
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4
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2
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5
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741913
Hoag
Bacterial renalase structure ...
Pseudomonas syringae 1448A, Pseudomonas syringae
Biochemistry
54
3791-3802
2015
-
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-
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-
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-
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8
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5
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1
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8
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3
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3
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8
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1
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8
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741920
Beaupre
Metabolic function for human ...
Homo sapiens
Biochemistry
54
795-806
2015
-
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-
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4
-
2
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6
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3
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3
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4
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6
-
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-
742685
Fedchenko
Human urinary renalase lacks ...
Homo sapiens
Int. J. Biol. Macromol.
78
347-353
2015
-
-
1
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-
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3
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2
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1
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1
1
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2
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-
743188
Li
Renalase protects the cardiom ...
Rattus norvegicus
Kidney Blood Press. Res.
40
215-222
2015
-
1
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3
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2
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1
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2
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1
1
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741902
Sonawane
Transcriptional regulation of ...
Homo sapiens
Biochemistry
53
6878-6892
2014
-
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1
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4
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4
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4
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2
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1
2
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4
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4
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742454
Quelhas-Santos
Plasma and urine renalase lev ...
Homo sapiens
Exp. Biol. Med. (Maywood)
239
502-508
2014
-
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2
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2
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1
1
1
1
-
-
743215
Li
Renalase, a new secretory enz ...
Homo sapiens
Med. Sci. Monit.
20
688-692
2014
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5
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2
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5
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5
1
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3
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3
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5
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5
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5
1
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1
1
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725209
Beaupre
Renalase is an alpha-NAD(P)H o ...
Homo sapiens
J. Am. Chem. Soc.
135
13980-13987
2013
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1
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1
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2
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1
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1
2
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1
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1
1
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1
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1
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1
2
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1
1
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726659
Sizova
Renalase regulates renal dopam ...
Mus musculus
Am. J. Physiol. Renal Physiol.
305
F839-F844
2013
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1
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727037
Beaupre
Kinetics and equilibria of the ...
Homo sapiens
Biochemistry
52
8929-8937
2013
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728281
Zhou
Expression and tissue localiza ...
Mus musculus
Mol. Biol. Rep.
40
3987-3994
2013
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7
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7
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2
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2
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728146
Milani
FAD-binding site and NADP reac ...
Homo sapiens
J. Mol. Biol.
411
463-473
2011
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1
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728036
Xu
Renalase is a novel, soluble m ...
Homo sapiens, Rattus norvegicus
J. Clin. Invest.
115
1275-1280
2005
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2
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